Yeast ornithine decarboxylase and antizyme form a 1:1 complex in vitro: Purification and characterization of the inhibitory complex

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Interactions of the human, plant and yeast ornithine decarboxylase subunits and human antizyme.

Introduction The small polycations known as polyamines (PAS) are intimately associated with cell proliferation and other important cellular processes such as translation and macromolecular stabilization [ 13. Consequently, PA metabolism and transport have been targeted for chemotherapeutic intervention during tumour development [2]. The first and key enzyme involved in PA synthesis is ornithine...

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Purification and some properties of a protein inhibitor (antizyme) of ornithine decarboxylase from rat liver.

A protein inhibitor to ornithine decarboxylase, antizyme, was purified to homogeneity, as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, about 600,000-fold with a 15% yield from the liver cytosol of putrescine-treated rats. Antizyme was very labile but markedly stabilized in the presence of Tween 80 and 2-mercaptoethanol. The apparent molecular weight of antizyme was deter...

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Ornithine decarboxylase antizyme in kidneys of male and female mice.

Antizyme, a protein inhibitor of ornithine decarboxylase (ODC), was shown to be induced in mouse kidney by repeated injection of putrescine. Antizyme was also present as a complex with ODC in the kidney of untreated mouse. The amount of the renal ODC-antizyme complex was 3-fold higher in male mice than in female mice. On the contrary, the proportion of ODC present as a complex with antizyme was...

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Minimal Antizyme Peptide Fully Functioning in the Binding and Inhibition of Ornithine Decarboxylase and Antizyme Inhibitor

Antizyme (AZ) is a protein with 228 amino acid residues that regulates ornithine decarboxylase (ODC) by binding to ODC and dissociating its homodimer, thus inhibiting its enzyme activity. Antizyme inhibitor (AZI) is homologous to ODC, but has a higher affinity than ODC for AZ. In this study, we quantified the biomolecular interactions between AZ and ODC as well as AZ and AZI to identify functio...

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A macromolecular inhibitor of the antizyme to ornithine decarboxylase.

A macromolecular factor that inhibits the activity of the antizyme to ornithine decarboxylase (ODC) was found in rat liver extracts. The factor, 'antizyme inhibitor', was heat-labile, non diffusable and of similar molecular size to ODC. The antizyme inhibitor re-activated ODC that had been inactivated by antizyme, apparently by replacing ODC in a complex with antizyme. Therefore the antizyme in...

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ژورنال

عنوان ژورنال: Biochemical and Biophysical Research Communications

سال: 2011

ISSN: 0006-291X

DOI: 10.1016/j.bbrc.2011.01.113